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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 2 (1975), S. 0 
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: An allotypic system of rabbit serum high density lipoprotein (HDL) has been reported previously from our laboratory. Homospecific rabbit sera revealed an antigen termed Hl 1, which is governed by autosomal dominant inheritance.An unexpected degree of cross-reactivity is described in this paper. Rabbit anti-Hl 1 sera were found to cross-react with a component present in pig serum. This component was found in all pig sera tested thus far, and there is therefore no evidence that it reflects an allotypic system in the pig.Fractionation in the preparative ultracentrifuge revealed that the component in pig serum resides in the HDL fraction. The antigenic resemblance between the component in pig serum and the rabbit Hl 1 antigen is considerable, as judged from experiments with antisera available at present. Immunological cross-reactivity of the described type may be more wide-spread than hitherto assumed.
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  • 2
    ISSN: 1546-170X
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] The mechanisms causing resistance to chemotherapeutic drugs in cancer patients are poorly understood. Recent evidence suggests that different forms of chemotherapy may exert their cytotoxic effects by inducing apoptosis1. The tumor suppressor gene P53 has a pivotal role inducing apoptosis in ...
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 5 (1978), S. 0 
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Purification and characterization of the Hl 1 antigen revealed a polypeptide with molecular weight of 20,000 by gel filtration. The peptide contained 20% neutral sugar and 4.5% neuraminic acid. Amino acid analysis as well as the Nterminal sequence for thirteen amino acid residues and three C-terminal amino acids were determined. Difference index analysis gave an indication that the H1 1 polypeptide is unique.Purification of R 67 antigen did not give a pure polypeptide in sufficient amount to do chemical analysis. A crude fraction of R 67 antigen had three bands on SDS-PAGE, all with R67 antigenic activity. The crude fraction contained 10% neutral sugar and 3.5% neuraminic acid. No N- or C-terminal amino acids could be determined for the crude fraction of R 67 antigen.
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 5 (1978), S. 0 
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Qualitative and quantitative analysis of the distribution of Hl 1 antigen and R 67 antigen on high density lipoprotein (HDL) particles were conducted on six rabbit sera. The Hl 1 antigen showed non-identity with A-I-containing HDL particles, and antiserum to Hl 1 did not remove A-I-containing HDL particles. The R 67 antigen showed partial identity with A-I-containing HDL particles. Antiserum to R 67 antigen removed 30–40% of A-I-containing HDL particles from the sera of animals which were heterozygous for R 67, and 65% of the A-I-containing HDL particles from the serum of one R 67 homozygous animal.
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  • 5
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 5 (1978), S. 0 
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Purfication of apoA-I from rabbit high density lipoproteins (HDL) gave one single band in sodium dodecylsulphate-polyacrylamide disc electrophoresis and reacted only with antiserum to apoA-I. The molecular weight was about 25000. The amino acid composition of rabbit apoA-I gave a difference index of 7.4 compared to human apoA-I and of 6.5 compared to dog apoA-I. Of the three carboxy terminal amino acid residues the rabbit protein has one in common with the dog.The amino acid sequence of twenty-nine amino terminal residues showed 62% homology with the human protein; a minimum of thirteen base changes were required in the DNA sequences that encoded these two proteins. When the same sequence was compared with dog apoA-I, it was found that ten base changes would be sufficient to account for the differences between the proteins.
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 4 (1977), S. 0 
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Antiserum to a rabbit HDL allotype has been produced in a sheep. Qualitative and quantitative immunological tests of whole rabbit serum and purified HDL polypeptides, as well as association tests, showed that the absorbed sheep immune serum reacts with the HDL allotype referred to as R 67.
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  • 7
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 4 (1977), S. 0 
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Close linkage between the two allotypic systems of rabbit serum high density lipoprotein (HDL), Hl 1 and R 67, has been confidently excluded, the recombination fraction being at least 0.20.No suggestion of linkage between either HDL allotype and the immunoglobulin allotypes a1a2a3/b4b9, or the red blood cell system (RBC) ADF was obtained.Close linkage was confidently excluded for the Hl 1–ADF, H1 1–a1a2a3, R 67–ADF, R 67–a1a2a3 R 67–b4b9, a1a2a3-b4 b9, and b4b9-ADF relationships.
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  • 8
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 3 (1976), S. 0 
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Rabbit high density lipoprotein (HDL) has been isolated by ultracentrifugation, delipidated by ether and ethanol, and treated with urea prior to separation of the different polypeptides by gel nitration. The two different genetic polymorphisms known in rabbit HDL were found to reside in two different polypeptides. This conclusion was reached in experiments where a quantitative radial immunodiffusion technique was employed. The results of polyacrylamide gel electrophoresis in SDS indicate that the H1 1 antigen resides in a polypeptide chain with a molecular weight of 40,000, whereas the R 67 antigen resides in a chain with a molecular weight of 17,000.
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  • 9
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 3 (1976), S. 0 
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Different classes of rabbit serum lipoprotein were prepared by ultracentrifugal flotation at densities 1·006, 1·063 and 1·21 g/ml. Agarose gel electrophoresis on rabbit whole serum and the serum fractions with different densities showed that this technique separates the different lipoprotein classes reasonably well.The electrophoretic mobility of the different lipoprotein classes of rabbit serum seems to be similar to that of the human lipoproteins, with the exception of α1-lipoprotein which had a greater mobility than human α1-lipoprotein.The chemical composition of rabbit high density lipoprotein (HDL) was fairly similar to that of human HDL although the former seems to be richer in triglycerides.HDL was, after isolation by ultracentrifugal flotation at density 1·21, delipidated and submitted to gel filtration on Sephadex G-200 in 8 m urea. The major protein fraction of rabbit apo HDL corresponds in elution volume to that of the major fraction of human apo HDL, apoA-I. A protein fraction corresponding to human apoA-II does not seem to be present in rabbit HDL in demonstrable amounts. The rabbit protein fraction sometimes appearing in the area corresponding to human apoA-II could not be found to be affected by the reduction and alkylation method after which humana poA-II splits into two identical chains.
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  • 10
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 3 (1976), S. 0 
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Immunological quantification of HDL and the inherited antigens H1 1 and R67 was performed on serum samples from two rabbit populations (Dutch and Albino) comprising a total of 106 animals. The female animals were found to have a higher concentration of both antigens and of HDL than the male animals. The amounts of antigens and of HDL were not obviously normally distributed, but appeared to be more bimodally distributed. The relationship between the amount of antigens and amount of HDL were tested for each animal. A significant positive correlation was found between the amount of R 67 antigen and HDL both for male and female animals in the Albino rabbit population, and for male animals in the Dutch rabbit population. A significant correlation was also found between amounts of H1 1 and R 67 antigens in the Dutch rabbit population.
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